Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method

Panchaporn Tadpitchayangkoon, Jae W. Park, Steven G. Mayer, Jirawat Yongsawatdigul

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Structural changes and dynamic rheological properties of sarcoplasmic proteins from striped catfish (Pangasius hypophthalmus) treated by various pH-shift processes were investigated. Isoelectric precipitation of acid-extracted sarcoplasmic proteins led to the lowest solubility in water. Sarcoplasmic proteins were unfolded after extremely acidic and alkaline extraction, exposing tryptophan and aliphatic residues. The α-helical structure was converted to β-sheet following acidic extraction, whereas alkaline treatment did not disturb the α-helical structure of sarcoplasmic proteins. Disulfide formation, hydrogen bonding via tyrosine residues, and hydrophobic interactions occurred under extreme pH extraction. Acidic extraction induced denaturation and aggregation of sarcoplasmic proteins to a greater extent than did alkaline treatment. Hydrophobic interactions via aliphatic and aromatic residues were formed during isoelectric precipitation. Sarcoplasmic proteins were partially refolded after isoelectric precipitation followed by neutralization. Sarcoplasmic proteins prepared from an alkaline pH-shift process readily aggregated to form a gel at 45.10 °C, whereas higher thermal denaturation temperatures (>80 °C) and gel points (∼78 °C) were observed in acid-treated sarcoplasmic proteins. The pH condition used for extraction, precipitation, and neutralization greatly affected structural changes of sarcoplasmic proteins, leading to different thermal and dynamic rheological properties.

Original languageEnglish
Pages (from-to)4241-4249
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Volume58
Issue number7
DOIs
Publication statusPublished - 2010 Apr 14
Externally publishedYes

Fingerprint

rheological properties
Proteins
proteins
Pangasianodon hypophthalmus
Denaturation
hydrophobic bonding
methodology
Hydrophobic and Hydrophilic Interactions
denaturation
neutralization
Hot Temperature
Gels
gels
Catfishes
Protein Unfolding
Acids
heat
hydrogen bonding
Hydrogen Bonding
acid deposition

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Chemistry(all)

Cite this

Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method. / Tadpitchayangkoon, Panchaporn; Park, Jae W.; Mayer, Steven G.; Yongsawatdigul, Jirawat.

In: Journal of Agricultural and Food Chemistry, Vol. 58, No. 7, 14.04.2010, p. 4241-4249.

Research output: Contribution to journalArticle

Tadpitchayangkoon, Panchaporn ; Park, Jae W. ; Mayer, Steven G. ; Yongsawatdigul, Jirawat. / Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method. In: Journal of Agricultural and Food Chemistry. 2010 ; Vol. 58, No. 7. pp. 4241-4249.
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